LEF1_HUMAN
ID LEF1_HUMAN Reviewed; 399 AA.
AC Q9UJU2; B4DG38; B7Z8E2; E9PDK3; Q3ZCU4; Q9HAZ0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Lymphoid enhancer-binding factor 1;
DE Short=LEF-1;
DE AltName: Full=T cell-specific transcription factor 1-alpha;
DE Short=TCF1-alpha;
GN Name=LEF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP FUNCTION.
RX PubMed=2010090; DOI=10.1101/gad.5.4.656;
RA Waterman M.L., Fischer W.H., Jones K.A.;
RT "A thymus-specific member of the HMG protein family regulates the human T
RT cell receptor C alpha enhancer.";
RL Genes Dev. 5:656-669(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=10756202; DOI=10.1093/nar/28.9.1994;
RA Hovanes K., Li T.W., Waterman M.L.;
RT "The human LEF-1 gene contains a promoter preferentially active in
RT lymphocytes and encodes multiple isoforms derived from alternative
RT splicing.";
RL Nucleic Acids Res. 28:1994-2003(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), ALTERNATIVE SPLICING,
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19653274; DOI=10.1002/ijc.24802;
RA Jesse S., Koenig A., Ellenrieder V., Menke A.;
RT "Lef-1 isoforms regulate different target genes and reduce cellular
RT adhesion.";
RL Int. J. Cancer 126:1109-1120(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RA Kobielak A., Kobielak K., Trzeciak W.H.;
RT "New transcript isoform of the human LEF-1 devoid of HMG domain, derived
RT from alternative splicing of exon 8.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7).
RC TISSUE=Amygdala, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
RC TISSUE=Skin, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP INTERACTION WITH ALYREF/THOC4.
RX PubMed=9119228; DOI=10.1101/gad.11.5.640;
RA Bruhn L., Munnerlyn A., Grosschedl R.;
RT "ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for
RT TCRalpha enhancer function.";
RL Genes Dev. 11:640-653(1997).
RN [10]
RP INTERACTION WITH CTNNB1.
RX PubMed=9488439; DOI=10.1128/mcb.18.3.1248;
RA Korinek V., Barker N., Willert K., Molenaar M., Roose J., Wagenaar G.,
RA Markman M., Lamers W., Destree O., Clevers H.;
RT "Two members of the Tcf family implicated in Wnt/b-catenin signaling during
RT embryogenesis in the mouse.";
RL Mol. Cell. Biol. 18:1248-1256(1998).
RN [11]
RP INTERACTION WITH TLE1, AND INHIBITION OF TRANSCRIPTIONAL ACTIVATION BY
RP TLE1.
RX PubMed=9751710; DOI=10.1073/pnas.95.20.11590;
RA Levanon D., Goldstein R.E., Bernstein Y., Tang H., Goldenberg D.,
RA Stifani S., Paroush Z., Groner Y.;
RT "Transcriptional repression by AML1 and LEF-1 is mediated by the
RT TLE/Groucho corepressors.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11590-11595(1998).
RN [12]
RP IDENTIFICATION (ISOFORM 3), FUNCTION, AND EXPRESSION IN COLON CANCER.
RX PubMed=11326276; DOI=10.1038/ng0501-53;
RA Hovanes K., Li T.W.H., Munguia J.E., Truong T., Milovanovic T.,
RA Lawrence Marsh J., Holcombe R.F., Waterman M.L.;
RT "Beta-catenin-sensitive isoforms of lymphoid enhancer factor-1 are
RT selectively expressed in colon cancer.";
RL Nat. Genet. 28:53-57(2001).
RN [13]
RP FUNCTIONAL INTERACTION WITH TLE1; TLE2; TLE3 AND TLE4.
RX PubMed=11266540; DOI=10.1093/nar/29.7.1410;
RA Brantjes H., Roose J., van De Wetering M., Clevers H.;
RT "All Tcf HMG box transcription factors interact with Groucho-related co-
RT repressors.";
RL Nucleic Acids Res. 29:1410-1419(2001).
RN [14]
RP INTERACTION WITH MDFI AND MDFIC.
RX PubMed=12192039; DOI=10.1128/mcb.22.18.6393-6405.2002;
RA Kusano S., Raab-Traub N.;
RT "I-mfa domain proteins interact with Axin and affect its regulation of the
RT Wnt and c-Jun N-terminal kinase signaling pathways.";
RL Mol. Cell. Biol. 22:6393-6405(2002).
RN [15]
RP INTERACTION WITH NLK, PHOSPHORYLATION AT THR-155 AND/OR SER-166 BY NLK, AND
RP MUTAGENESIS OF THR-155 AND SER-166.
RX PubMed=12556497; DOI=10.1128/mcb.23.4.1379-1389.2003;
RA Ishitani T., Ninomiya-Tsuji J., Matsumoto K.;
RT "Regulation of lymphoid enhancer factor 1/T-cell factor by mitogen-
RT activated protein kinase-related Nemo-like kinase-dependent phosphorylation
RT in Wnt/beta-catenin signaling.";
RL Mol. Cell. Biol. 23:1379-1389(2003).
RN [16]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-113.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Transcription factor that binds DNA in a sequence-specific
CC manner (PubMed:2010090). Participates in the Wnt signaling pathway (By
CC similarity). Activates transcription of target genes in the presence of
CC CTNNB1 and EP300 (By similarity). PIAG antagonizes both Wnt-dependent
CC and Wnt-independent activation by LEF1 (By similarity). TLE1, TLE2,
CC TLE3 and TLE4 repress transactivation mediated by LEF1 and CTNNB1
CC (PubMed:11266540). Regulates T-cell receptor alpha enhancer function
CC (PubMed:19653274). Required for IL17A expressing gamma-delta T-cell
CC maturation and development, via binding to regulator loci of BLK to
CC modulate expression (By similarity). May play a role in hair cell
CC differentiation and follicle morphogenesis (By similarity).
CC {ECO:0000250|UniProtKB:P27782, ECO:0000269|PubMed:11266540,
CC ECO:0000269|PubMed:19653274, ECO:0000269|PubMed:2010090}.
CC -!- FUNCTION: [Isoform 1]: Transcriptionally activates MYC and CCND1
CC expression and enhances proliferation of pancreatic tumor cells.
CC {ECO:0000269|PubMed:19653274}.
CC -!- FUNCTION: [Isoform 3]: Lacks the CTNNB1 interaction domain and may
CC therefore be an antagonist for Wnt signaling.
CC {ECO:0000269|PubMed:11326276}.
CC -!- FUNCTION: [Isoform 5]: Transcriptionally activates the fibronectin
CC promoter, binds to and represses transcription from the E-cadherin
CC promoter in a CTNNB1-independent manner, and is involved in reducing
CC cellular aggregation and increasing cell migration of pancreatic cancer
CC cells. {ECO:0000269|PubMed:19653274}.
CC -!- SUBUNIT: Binds the armadillo repeat of CTNNB1 and forms a stable
CC complex. Interacts with EP300, TLE1 and PIASG (By similarity). Binds
CC ALYREF/THOC4, MDFI and MDFIC. Interacts with NLK. {ECO:0000250,
CC ECO:0000269|PubMed:12192039, ECO:0000269|PubMed:12556497,
CC ECO:0000269|PubMed:9119228, ECO:0000269|PubMed:9488439,
CC ECO:0000269|PubMed:9751710}.
CC -!- INTERACTION:
CC Q9UJU2; P35222: CTNNB1; NbExp=10; IntAct=EBI-926131, EBI-491549;
CC Q9UJU2; P49789: FHIT; NbExp=2; IntAct=EBI-926131, EBI-741760;
CC Q9UJU2; P08069: IGF1R; NbExp=5; IntAct=EBI-926131, EBI-475981;
CC Q9UJU2; Q16236: NFE2L2; NbExp=3; IntAct=EBI-926131, EBI-2007911;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC Note=Found in nuclear bodies upon PIASG binding. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=A;
CC IsoId=Q9UJU2-1; Sequence=Displayed;
CC Name=2; Synonyms=B, 8A;
CC IsoId=Q9UJU2-2; Sequence=VSP_002188;
CC Name=3; Synonyms=LEF-1-DN;
CC IsoId=Q9UJU2-3; Sequence=VSP_007022;
CC Name=4;
CC IsoId=Q9UJU2-4; Sequence=VSP_007022, VSP_002188;
CC Name=5;
CC IsoId=Q9UJU2-5; Sequence=VSP_040068;
CC Name=6;
CC IsoId=Q9UJU2-6; Sequence=VSP_040068, VSP_040069;
CC Name=7;
CC IsoId=Q9UJU2-7; Sequence=VSP_044877, VSP_040068;
CC -!- TISSUE SPECIFICITY: Detected in thymus. Not detected in normal colon,
CC but highly expressed in colon cancer biopsies and colon cancer cell
CC lines. Expressed in several pancreatic tumors and weakly expressed in
CC normal pancreatic tissue. Isoforms 1 and 5 are detected in several
CC pancreatic cell lines. {ECO:0000269|PubMed:19653274}.
CC -!- DOMAIN: Proline-rich and acidic regions are implicated in the
CC activation functions of RNA polymerase II transcription factors.
CC -!- PTM: Phosphorylated at Thr-155 and/or Ser-166 by NLK. Phosphorylation
CC by NLK at these sites represses LEF1-mediated transcriptional
CC activation of target genes of the canonical Wnt signaling pathway.
CC {ECO:0000269|PubMed:12556497}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform
CC 1. May be produced at very low levels due to a premature stop codon in
CC the mRNA, leading to nonsense-mediated mRNA decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
CC Acts as dominant negative mutant. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform
CC 3. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TCF/LEF family. {ECO:0000305}.
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DR EMBL; AF288571; AAG01022.1; -; mRNA.
DR EMBL; AF198532; AAF13268.1; -; mRNA.
DR EMBL; AF294627; AAG26886.1; -; mRNA.
DR EMBL; AK294395; BAG57649.1; -; mRNA.
DR EMBL; AK303272; BAH13928.1; -; mRNA.
DR EMBL; AC092539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC097067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC118062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC123576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX06223.1; -; Genomic_DNA.
DR EMBL; CH471057; EAX06225.1; -; Genomic_DNA.
DR EMBL; BC040559; AAH40559.1; -; mRNA.
DR EMBL; BC050632; AAH50632.1; -; mRNA.
DR CCDS; CCDS3679.1; -. [Q9UJU2-1]
DR CCDS; CCDS47122.1; -. [Q9UJU2-6]
DR CCDS; CCDS47123.1; -. [Q9UJU2-5]
DR CCDS; CCDS54791.1; -. [Q9UJU2-7]
DR PIR; A39625; A39625.
DR RefSeq; NP_001124185.1; NM_001130713.2. [Q9UJU2-5]
DR RefSeq; NP_001124186.1; NM_001130714.2. [Q9UJU2-6]
DR RefSeq; NP_001159591.1; NM_001166119.1. [Q9UJU2-7]
DR RefSeq; NP_057353.1; NM_016269.4. [Q9UJU2-1]
DR AlphaFoldDB; Q9UJU2; -.
DR BMRB; Q9UJU2; -.
DR SMR; Q9UJU2; -.
DR BioGRID; 119354; 57.
DR ComplexPortal; CPX-316; beta1-catenin - LEF1 complex.
DR CORUM; Q9UJU2; -.
DR DIP; DIP-29946N; -.
DR IntAct; Q9UJU2; 26.
DR MINT; Q9UJU2; -.
DR STRING; 9606.ENSP00000265165; -.
DR ChEMBL; CHEMBL3217392; -.
DR DrugBank; DB00903; Etacrynic acid.
DR GlyConnect; 2055; 1 N-Linked glycan (1 site).
DR GlyGen; Q9UJU2; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q9UJU2; -.
DR PhosphoSitePlus; Q9UJU2; -.
DR BioMuta; LEF1; -.
DR DMDM; 8928194; -.
DR EPD; Q9UJU2; -.
DR jPOST; Q9UJU2; -.
DR MassIVE; Q9UJU2; -.
DR MaxQB; Q9UJU2; -.
DR PaxDb; Q9UJU2; -.
DR PeptideAtlas; Q9UJU2; -.
DR PRIDE; Q9UJU2; -.
DR ProteomicsDB; 19686; -.
DR ProteomicsDB; 84650; -. [Q9UJU2-1]
DR ProteomicsDB; 84651; -. [Q9UJU2-2]
DR ProteomicsDB; 84652; -. [Q9UJU2-3]
DR ProteomicsDB; 84653; -. [Q9UJU2-4]
DR ProteomicsDB; 84654; -. [Q9UJU2-5]
DR ProteomicsDB; 84655; -. [Q9UJU2-6]
DR TopDownProteomics; Q9UJU2-2; -. [Q9UJU2-2]
DR Antibodypedia; 912; 810 antibodies from 45 providers.
DR DNASU; 51176; -.
DR Ensembl; ENST00000265165.6; ENSP00000265165.1; ENSG00000138795.10. [Q9UJU2-1]
DR Ensembl; ENST00000379951.6; ENSP00000369284.2; ENSG00000138795.10. [Q9UJU2-6]
DR Ensembl; ENST00000438313.6; ENSP00000406176.2; ENSG00000138795.10. [Q9UJU2-5]
DR Ensembl; ENST00000506680.5; ENSP00000422334.1; ENSG00000138795.10. [Q9UJU2-2]
DR Ensembl; ENST00000510624.5; ENSP00000422840.1; ENSG00000138795.10. [Q9UJU2-7]
DR GeneID; 51176; -.
DR KEGG; hsa:51176; -.
DR MANE-Select; ENST00000265165.6; ENSP00000265165.1; NM_016269.5; NP_057353.1.
DR UCSC; uc003hyt.3; human. [Q9UJU2-1]
DR CTD; 51176; -.
DR DisGeNET; 51176; -.
DR GeneCards; LEF1; -.
DR HGNC; HGNC:6551; LEF1.
DR HPA; ENSG00000138795; Tissue enriched (lymphoid).
DR MIM; 153245; gene.
DR neXtProt; NX_Q9UJU2; -.
DR OpenTargets; ENSG00000138795; -.
DR PharmGKB; PA30331; -.
DR VEuPathDB; HostDB:ENSG00000138795; -.
DR eggNOG; KOG3248; Eukaryota.
DR GeneTree; ENSGT00940000159660; -.
DR HOGENOM; CLU_013229_5_0_1; -.
DR InParanoid; Q9UJU2; -.
DR OMA; NFSTCKA; -.
DR OrthoDB; 807716at2759; -.
DR PhylomeDB; Q9UJU2; -.
DR TreeFam; TF318448; -.
DR PathwayCommons; Q9UJU2; -.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-4411364; Binding of TCF/LEF:CTNNB1 to target gene promoters.
DR Reactome; R-HSA-4641265; Repression of WNT target genes.
DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-HSA-8951430; RUNX3 regulates WNT signaling.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR SignaLink; Q9UJU2; -.
DR SIGNOR; Q9UJU2; -.
DR BioGRID-ORCS; 51176; 9 hits in 1101 CRISPR screens.
DR ChiTaRS; LEF1; human.
DR GeneWiki; Lymphoid_enhancer-binding_factor_1; -.
DR GenomeRNAi; 51176; -.
DR Pharos; Q9UJU2; Tchem.
DR PRO; PR:Q9UJU2; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9UJU2; protein.
DR Bgee; ENSG00000138795; Expressed in thymus and 178 other tissues.
DR ExpressionAtlas; Q9UJU2; baseline and differential.
DR Genevisible; Q9UJU2; HS.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IPI:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; IDA:BHF-UCL.
DR GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0070016; F:armadillo repeat domain binding; IPI:BHF-UCL.
DR GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0008301; F:DNA binding, bending; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:BHF-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0045295; F:gamma-catenin binding; IPI:BHF-UCL.
DR GO; GO:0042393; F:histone binding; IPI:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:GO_Central.
DR GO; GO:0060033; P:anatomical structure regression; IEA:Ensembl.
DR GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; IMP:BHF-UCL.
DR GO; GO:0071353; P:cellular response to interleukin-4; IDA:UniProtKB.
DR GO; GO:0060710; P:chorio-allantoic fusion; IEA:Ensembl.
DR GO; GO:0021542; P:dentate gyrus development; IEA:Ensembl.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
DR GO; GO:1904019; P:epithelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:BHF-UCL.
DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR GO; GO:0021873; P:forebrain neuroblast division; IEA:Ensembl.
DR GO; GO:0021861; P:forebrain radial glial cell differentiation; IEA:Ensembl.
DR GO; GO:0021943; P:formation of radial glial scaffolds; IEA:Ensembl.
DR GO; GO:0043966; P:histone H3 acetylation; IMP:UniProtKB.
DR GO; GO:0097043; P:histone H3-K56 acetylation; IEA:Ensembl.
DR GO; GO:0043967; P:histone H4 acetylation; IMP:UniProtKB.
DR GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0071866; P:negative regulation of apoptotic process in bone marrow cell; IMP:UniProtKB.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:0032696; P:negative regulation of interleukin-13 production; IDA:UniProtKB.
DR GO; GO:0032713; P:negative regulation of interleukin-4 production; IDA:UniProtKB.
DR GO; GO:0032714; P:negative regulation of interleukin-5 production; IDA:UniProtKB.
DR GO; GO:0045843; P:negative regulation of striated muscle tissue development; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030223; P:neutrophil differentiation; IMP:UniProtKB.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEP:UniProtKB.
DR GO; GO:0048341; P:paraxial mesoderm formation; IEA:Ensembl.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:UniProtKB.
DR GO; GO:0090068; P:positive regulation of cell cycle process; IDA:UniProtKB.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; IMP:UniProtKB.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; IEA:Ensembl.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR GO; GO:0030854; P:positive regulation of granulocyte differentiation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0050767; P:regulation of neurogenesis; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0062009; P:secondary palate development; ISS:BHF-UCL.
DR GO; GO:0050909; P:sensory perception of taste; IEA:Ensembl.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0002040; P:sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0033153; P:T cell receptor V(D)J recombination; IEA:Ensembl.
DR GO; GO:0045063; P:T-helper 1 cell differentiation; ISS:UniProtKB.
DR GO; GO:0043586; P:tongue development; IEA:Ensembl.
DR GO; GO:0061153; P:trachea gland development; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR013558; CTNNB1-bd_N.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR028769; LEF1.
DR InterPro; IPR024940; TCF/LEF.
DR PANTHER; PTHR10373; PTHR10373; 1.
DR PANTHER; PTHR10373:SF11; PTHR10373:SF11; 1.
DR Pfam; PF08347; CTNNB1_binding; 1.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative promoter usage; Alternative splicing;
KW Direct protein sequencing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..399
FT /note="Lymphoid enhancer-binding factor 1"
FT /id="PRO_0000048595"
FT DNA_BIND 299..367
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..62
FT /note="CTNNB1-binding"
FT /evidence="ECO:0000250"
FT REGION 166..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 155
FT /note="Phosphothreonine; by NLK"
FT /evidence="ECO:0000305|PubMed:12556497"
FT MOD_RES 166
FT /note="Phosphoserine; by NLK"
FT /evidence="ECO:0000305|PubMed:12556497"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 269
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..115
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_007022"
FT VAR_SEQ 1..70
FT /note="MPQLSGGGGGGGGDPELCATDEMIPFKDEGDPQKEKIFAEISHPEEEGDLAD
FT IKSSLVNESEIIPASNGH -> MA (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044877"
FT VAR_SEQ 214..241
FT /note="Missing (in isoform 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:19653274"
FT /id="VSP_040068"
FT VAR_SEQ 283..399
FT /note="KPQHEQRKEQEPKRPHIKKPLNAFMLYMKEMRANVVAECTLKESAAINQILG
FT RRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKREKLQESASGTGPR
FT MTAAYI -> CSAFLLPHPFLIPSTPSPNHHHHHLLGSLSMNRERSRSQKDLTLRSL
FT (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_002188"
FT VAR_SEQ 390..399
FT /note="TGPRMTAAYI -> GKRSSFPTCKAKAATPGPLLEMEAC (in isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040069"
FT VARIANT 113
FT /note="G -> R (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs369649181)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035935"
FT MUTAGEN 155
FT /note="T->A: Reduced phosphorylation by NLK; when
FT associated with A-166."
FT /evidence="ECO:0000269|PubMed:12556497"
FT MUTAGEN 166
FT /note="S->A: Reduced phosphorylation by NLK; when
FT associated with A-155."
FT /evidence="ECO:0000269|PubMed:12556497"
FT CONFLICT 146
FT /note="Q -> R (in Ref. 5; BAH13928)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 44201 MW; D480D440698EEFE3 CRC64;
MPQLSGGGGG GGGDPELCAT DEMIPFKDEG DPQKEKIFAE ISHPEEEGDL ADIKSSLVNE
SEIIPASNGH EVARQAQTSQ EPYHDKAREH PDDGKHPDGG LYNKGPSYSS YSGYIMMPNM
NNDPYMSNGS LSPPIPRTSN KVPVVQPSHA VHPLTPLITY SDEHFSPGSH PSHIPSDVNS
KQGMSRHPPA PDIPTFYPLS PGGVGQITPP LGWQGQPVYP ITGGFRQPYP SSLSVDTSMS
RFSHHMIPGP PGPHTTGIPH PAIVTPQVKQ EHPHTDSDLM HVKPQHEQRK EQEPKRPHIK
KPLNAFMLYM KEMRANVVAE CTLKESAAIN QILGRRWHAL SREEQAKYYE LARKERQLHM
QLYPGWSARD NYGKKKKRKR EKLQESASGT GPRMTAAYI
